Self-assembly of peptide nanofibers and their mechanical properties

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buir.advisorGüler, Mustafa Özgür
dc.contributor.authorErkal, Turan Selman
dc.date.accessioned2016-01-08T18:19:38Z
dc.date.available2016-01-08T18:19:38Z
dc.date.issued2012
dc.descriptionAnkara : The Materials Science and Nanotechnology Program of the Graduate School of Engineering and Science of Bilkent University, 2012.en_US
dc.descriptionThesis (Master's) -- Bilkent University, 2012.en_US
dc.descriptionIncludes bibliographical references leaves 80-82.en_US
dc.description.abstractPeptide nanofibers have been drawing attention because of their versatile, tailorable and functional properties in various research areas. The self-assembly mechanism of peptides and peptide amphiphile molecules is generally based on noncovalent interactions like hydrophobic, electrostatic and metal-ligand interactions. In this thesis, I investigated hydrophobic interaction of peptide amphiphiles (PAs) with other hydrophobic molecules and effect of pH change on self-assembly mechanism. The zinc phthalocyanine molecule was used as a hydrophobic probe to be encapsulated by peptide amphiphile molecules, which help to dissolve the molecule in water instead of an organic solvent. Charge neutralization of PAs by pH change led to nanofiber formation, which resulted in encapsulation and organization of zinc phthalocyanine molecules. The degree of self-assembly by pH change determined non-linear optical properties of zinc phthalocyanine molecule. Besides, morphological, mechanical and spectroscopic properties of phthalocyanine containing peptide nanofibers were characterized by TEM, SEM, oscillatory rheology, UV-Vis, fluorescence and circular dichroism spectroscopy. The mechanical properties of peptide and PA hydrogels and nanofibers have an essential place to determine applicability in different areas. Especially, PA and peptide molecules have been widely used in regenerative medicine studies and the stiffness of the extracellular matrix has a significant role on cellular behavior. In this thesis, viscoelastic properties of the peptide and PA gels were studied by oscillatory rheology. In addition to characterization of bulk mechanical properties of peptide gels, adhesion and stiffness of peptide nanofibers were determined by Atomic Force Microscopy.en_US
dc.description.provenanceMade available in DSpace on 2016-01-08T18:19:38Z (GMT). No. of bitstreams: 1 0006243.pdf: 2031977 bytes, checksum: 7a57a62677f0a5d32db7ff8fe767004f (MD5)en
dc.description.statementofresponsibilityErkal, Turan Selmanen_US
dc.format.extentxiv, 82 leaves, illustrationsen_US
dc.identifier.urihttp://hdl.handle.net/11693/15509
dc.language.isoEnglishen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectPeptide nanofiberen_US
dc.subjectself-assemblyen_US
dc.subjectencapsulationen_US
dc.subjectzinc phthalocyanineen_US
dc.subjectrheologyen_US
dc.subjectAtomic Force Microscopyen_US
dc.subjectnanomechanical propertiesen_US
dc.subject.lccQP552.P4 E75 2012en_US
dc.subject.lcshPeptides--Synthesis.en_US
dc.subject.lcshNanostructured materials.en_US
dc.titleSelf-assembly of peptide nanofibers and their mechanical propertiesen_US
dc.typeThesisen_US
thesis.degree.disciplineMaterials Science and Nanotechnology
thesis.degree.grantorBilkent University
thesis.degree.levelMaster's
thesis.degree.nameMS (Master of Science)

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